Expression and genomic structure of the genes encoding FdI, the major allergen from the domestic cat

Recognition of the Major Cat Allergen Fel d 1 through the Cysteine-rich Domain of the Mannose Receptor Determines Its Allergenicity

“…Fel d 1 is a 35-kDa tetrameric glycoprotein formed by two heterodimers. Each dimer is composed of two chains (chain 1 and 2) derived from two independent genes (38,39). In agreement with the primary amino acid sequence predicting a single N-glycosylation site at Asn 33 , we identified the single glycopeptide VNATEPER within Fel d 1 (Fig.…”

Cloning of a Syrian hamster cDNA related to sexual dimorphism: establishment of a new family of proteins

“…The hamster cDNA clone FHG22, isolated from female HG, is similar to the subunits from several oligomeric secreted proteins, the functions of which have not yet been clarified: rat prostatein or prostatic steroid binding protein (PSBP) [9], uteroglobin (UG) [10] or Clara cell 10 KDa protein (CC10) [11] from different species, chain 1 of the major cat allergen Fel dI (Fdl 1) and ~ subunit from the mouse salivary androgen binding proteins (msABP ~) [12]. Sequence similarities between PSBP and UG [13] and between UG, FdI 1 and msABP ~ have been reported [11,14], while the genes for PSBR UG and FdI 1 show a common structure [15,16,17,18,19]. In addition, it has been described that PSBP and msABP bind steroids [9,12,15], while UG/CC10 also binds other ligands [10,20,21].…”

Formation of Disulfide Bonds and Homodimers of the Major Cat Allergen Fel d 1 Equivalent to the Natural Allergen by Expression in Escherichia coli

“…It is formed by two non-covalently linked heterodimers (16), each consisting of one 70-residue peptide and one 85- (22), 90-, or 92-residue peptide (17) (i.e. chain 1 and chain 2, respectively) encoded by separate genes (22,27). Chain 1 shares limited sequence homology with the rabbit uteroglobulin/human Clara cell 10-kDa protein (28,29), and the mature natural Fel d 1 (nFel d 1) 1 has been associated with gelatin-and fibronectin-degrading activity (30).…”